CGOX_MYCBO
ID CGOX_MYCBO Reviewed; 452 AA.
AC P0A5A8; A0A1R3Y1V5; O53230; X2BLI7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Coproporphyrinogen III oxidase {ECO:0000250|UniProtKB:P32397};
DE EC=1.3.3.15 {ECO:0000250|UniProtKB:P32397};
GN Name=cgoX {ECO:0000250|UniProtKB:P32397}; Synonyms=hemY;
GN OrderedLocusNames=BQ2027_MB2696C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- FUNCTION: Involved in coproporphyrin-dependent heme b biosynthesis.
CC Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin
CC III. {ECO:0000250|UniProtKB:P32397}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2;
CC Xref=Rhea:RHEA:43436, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57309, ChEBI:CHEBI:131725; EC=1.3.3.15;
CC Evidence={ECO:0000250|UniProtKB:P32397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43437;
CC Evidence={ECO:0000250|UniProtKB:P32397};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P32397};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P32397};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoheme
CC biosynthesis. {ECO:0000250|UniProtKB:P32397}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P32397}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Coproporphyrinogen III oxidase subfamily.
CC {ECO:0000305}.
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DR EMBL; LT708304; SIU01314.1; -; Genomic_DNA.
DR RefSeq; NP_856342.1; NC_002945.3.
DR RefSeq; WP_003413871.1; NC_002945.4.
DR AlphaFoldDB; P0A5A8; -.
DR SMR; P0A5A8; -.
DR EnsemblBacteria; SIU01314; SIU01314; BQ2027_MB2696C.
DR PATRIC; fig|233413.5.peg.2955; -.
DR OMA; EHNQAVQ; -.
DR UniPathway; UPA00252; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:InterPro.
DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR00562; proto_IX_ox; 1.
PE 3: Inferred from homology;
KW Cytoplasm; FAD; Flavoprotein; Heme biosynthesis; Oxidoreductase.
FT CHAIN 1..452
FT /note="Coproporphyrinogen III oxidase"
FT /id="PRO_0000135266"
FT BINDING 10..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 36..37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 58..61
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 242
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P56601"
FT BINDING 390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
FT BINDING 426..428
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P32397"
SQ SEQUENCE 452 AA; 46846 MW; 6DFA1F57BEE2810F CRC64;
MTPRSYCVVG GGISGLTSAY RLRQAVGDDA TITLFEPADR LGGVLRTEHI GGQPMDLGAE
AFVLRRPEMP ALLAELGLSD RQLASTGARP LIYSQQRLHP LPPQTVVGIP SSAGSMAGLV
DDATLARIDA EAARPFTWQV GSDPAVADLV ADRFGDQVVA RSVDPLLSGV YAGSAATIGL
RAAAPSVAAA LDRGATSVTD AVRQALPPGS GGPVFGALDG GYQVLLDGLV RRSRVHWVRA
RVVQLERGWV LRDETGGRWQ ADAVILAVPA PRLARLVDGI APRTHAAARQ IVSASSAVVA
LAVPGGTAFP HCSGVLVAGD ESPHAKAITL SSRKWGQRGD VALLRLSFGR FGDEPALTAS
DDQLLAWAAD DLVTVFGVAV DPVDVRVRRW IEAMPQYGPG HADVVAELRA GLPPTLAVAG
SYLDGIGVPA CVGAAGRAVT SVIEALDAQV AR
